Type |
Details |
Score |
Publication |
First Author: |
Adams DJ |
Year: |
2024 |
Journal: |
Nature |
Title: |
Genetic determinants of micronucleus formation in vivo. |
Volume: |
627 |
Issue: |
8002 |
Pages: |
130-136 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
First Author: |
GemPharmatech |
Year: |
2020 |
|
Title: |
GemPharmatech Website. |
|
|
|
|
•
•
•
•
•
|
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 |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
UniProt-GOA |
Year: |
2012 |
|
Title: |
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
GOA curators |
Year: |
2016 |
|
Title: |
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
The Jackson Laboratory Mouse Radiation Hybrid Database |
Year: |
2004 |
Journal: |
Database Release |
Title: |
Mouse T31 Radiation Hybrid Data Load |
|
|
|
|
•
•
•
•
•
|
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: |
MGI Genome Annotation Group and UniGene Staff |
Year: |
2015 |
Journal: |
Database Download |
Title: |
MGI-UniGene Interconnection Effort |
|
|
|
|
•
•
•
•
•
|
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 |
|
|
|
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
587
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
545
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
560
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
591
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
583
 |
Fragment?: |
false |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Folylpolyglutamate synthase (FPGS) is an ATP-dependent enzyme that is responsible for the addition of a polyglutamate tail to folate and folate derivatives []. It plays a key role in the retention of the intracellular folate pool. In some bacteria, such as Escherichia coli, the addition of L-glutamate to dihydropteroate (dihydrofolate synthetase activity) and the subsequent additions of L-glutamate to tetrahydrofolate (FPGS activity) are catalyzed by the same enzyme, FolC [].The crystal structure of the MgATP complex of the enzyme from Lactobacillus casei reveals FPGS to be a modular protein, consisting of two domains, one with a typical mononucleotide-binding fold and the other similar to the folate-binding enzyme dihydrofolate reductase. The active site of the enzyme is located in a large interdomain cleft adjacent to an ATP-binding P-loop motif. Opposite this site, in the C domain, a cavity likely to be the folate binding site has been identified, and inspection of this cavity and the surrounding protein structure suggests that the glutamate tail of the substrate may project into the active site. A further feature of the structure is a well defined Omega loop, which contributes both to the active site and to interdomain interactions [].This entry represents the eukaryotic FPGS enzymes. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Conserved_site |
Description: |
Folylpolyglutamate synthase (FPGS) is an ATP-dependent enzyme that is responsible for the addition of a polyglutamate tail to folate and folate derivatives []. It plays a key role in the retention of the intracellular folate pool. In some bacteria, such as Escherichia coli, the addition of L-glutamate to dihydropteroate (dihydrofolate synthetase activity) and the subsequent additions of L-glutamate to tetrahydrofolate (FPGS activity) are catalyzed by the same enzyme, FolC [].The crystal structure of the MgATP complex of the enzyme from Lactobacillus casei reveals FPGS to be a modular protein, consisting of two domains, one with a typical mononucleotide-binding fold and the other similar to the folate-binding enzyme dihydrofolate reductase. The active site of the enzyme is located in a large interdomain cleft adjacent to an ATP-binding P-loop motif. Opposite this site, in the C domain, a cavity likely to be the folate binding site has been identified, and inspection of this cavity and the surrounding protein structure suggests that the glutamate tail of the substrate may project into the active site. A further feature of the structure is a well defined Omega loop, which contributes both to the active site and to interdomain interactions [].This entry represents a conserved site found in the FPGS enzymes. |
|
•
•
•
•
•
|
Publication |
First Author: |
Sun X |
Year: |
1998 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase. |
Volume: |
95 |
Issue: |
12 |
Pages: |
6647-52 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mathieu M |
Year: |
2005 |
Journal: |
J Biol Chem |
Title: |
Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy. |
Volume: |
280 |
Issue: |
19 |
Pages: |
18916-22 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
243
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
189
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Folylpolyglutamate synthase (FPGS) is an ATP-dependent enzyme that is responsible for the addition of a polyglutamate tail to folate and folate derivatives []. It plays a key role in the retention of the intracellular folate pool. In some bacteria, such as Escherichia coli, the addition of L-glutamate to dihydropteroate (dihydrofolate synthetase activity) and the subsequent additions of L-glutamate to tetrahydrofolate (FPGS activity) are catalyzed by the same enzyme, FolC [].The crystal structure of the MgATP complex of the enzyme from Lactobacillus casei reveals FPGS to be a modular protein, consisting of two domains, one with a typical mononucleotide-binding fold and the other similar to the folate-binding enzyme dihydrofolate reductase. The active site of the enzyme is located in a large interdomain cleft adjacent to an ATP-binding P-loop motif. Opposite this site, in the C domain, a cavity likely to be the folate binding site has been identified, and inspection of this cavity and the surrounding protein structure suggests that the glutamate tail of the substrate may project into the active site. A further feature of the structure is a well defined Omega loop, which contributes both to the active site and to interdomain interactions []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Freemantle SJ |
Year: |
1997 |
Journal: |
J Biol Chem |
Title: |
Transcription of the human folylpoly-gamma-glutamate synthetase gene. |
Volume: |
272 |
Issue: |
40 |
Pages: |
25373-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Barton DE |
Year: |
1987 |
Journal: |
Cytogenet Cell Genet |
Title: |
NEAS encoding a non-erthyroid alpha-spectrin is on Chromosome 9, region q33-q34 and on mouse Chromosome 2. |
Volume: |
46 |
|
Pages: |
578 (Abstr.) |
|
•
•
•
•
•
|