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Search results 201 to 255 out of 255 for Bpgm

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Type Details Score
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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DO Term
DOID:0111630 | familial erythrocytosis 8
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Protein
P15327
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: false
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GO Term
GO:0004082 | bisphosphoglycerate mutase activity
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Publication
34138843 | J:342569
First Author: Qiang Q
Year: 2021
Journal: PLoS Biol
Title: Erythrocyte adenosine A2B receptor prevents cognitive and auditory dysfunction by promoting hypoxic and metabolic reprogramming.
Volume: 19
Issue: 6
Pages: e3001239
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Publication
2831102 | -
First Author: White MF
Year: 1988
Journal: FEBS Lett
Title: Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae.
Volume: 229
Issue: 2
Pages: 383-7
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Publication
7929373 | -
First Author: O'Toole GA
Year: 1994
Journal: J Biol Chem
Title: The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin.
Volume: 269
Issue: 42
Pages: 26503-11
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Publication
6294454 | -
 
First Author: Rose ZB
Year: 1982
Journal: Methods Enzymol
Title: Intermediates in the phosphoglycerate mutase and bisphosphoglycerate synthase reactions.
Volume: 87
Pages: 42-51
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Publication
2557623 | -
First Author: Bazan JF
Year: 1989
Journal: Proc Natl Acad Sci U S A
Title: Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.
Volume: 86
Issue: 24
Pages: 9642-6
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Protein Domain
IPR001345 | PG/BPGM_mutase_AS
Type: Active_site
Description: Phosphoglycerate mutase () (PGAM) and bisphosphoglycerate mutase () (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate [, , ]. Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity).In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.BPGM is a dimeric protein and is found mainly in erythrocytes where it plays a major role in regulating haemoglobin oxygen affinity as a consequence of controlling 2,3-DPG concentration. The catalytic mechanism of both PGAM and BPGM involves the formation of a phosphohistidine intermediate [].A number of other proteins including, the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase []that catalyses both the synthesis and the degradation of fructose-2,6-bisphosphate and bacterial alpha-ribazole-5'-phosphate phosphatase, which is involved in cobalamin biosynthesis, belong to this family [].This entry contains the active site phosphohistidine residue.
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Publication
10958932 | -
First Author: Jedrzejas MJ
Year: 2000
Journal: Prog Biophys Mol Biol
Title: Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase.
Volume: 73
Issue: 2-4
Pages: 263-87
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Protein
Q9DBJ1
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: false
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Protein
Q8BZA9
Organism: Mus musculus/domesticus
Length: 269  
Fragment?: false
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Protein
O70250
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: false
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Protein
Q5NCI4
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: false
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Protein
D3YUE8
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: true
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Protein
D3Z223
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: true
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Protein
Q3TAQ8
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: false
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Protein
D3YYH3
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: true
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Protein
B2RWB7
Organism: Mus musculus/domesticus
Length: 269  
Fragment?: false
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Protein
Q3U7Z6
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: false
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Protein
P70266
Organism: Mus musculus/domesticus
Length: 471  
Fragment?: false
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Protein
P70265
Organism: Mus musculus/domesticus
Length: 519  
Fragment?: false
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Protein
Q6DTY7
Organism: Mus musculus/domesticus
Length: 469  
Fragment?: false
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Protein
A0A0A6YY64
Organism: Mus musculus/domesticus
Length: 500  
Fragment?: false
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Protein
A2AFM9
Organism: Mus musculus/domesticus
Length: 448  
Fragment?: false
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Protein
A7UAK8
Organism: Mus musculus/domesticus
Length: 543  
Fragment?: false
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Protein
Q3U3S6
Organism: Mus musculus/domesticus
Length: 549  
Fragment?: false
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Protein
B2Z892
Organism: Mus musculus/domesticus
Length: 497  
Fragment?: false
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Protein
A2AUP4
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: false
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Protein
C9VZF3
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
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Protein
C9VZF2
Organism: Mus musculus/domesticus
Length: 435  
Fragment?: false
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Protein
Q9ESY2
Organism: Mus musculus/domesticus
Length: 520  
Fragment?: false
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Protein
A2AUP1
Organism: Mus musculus/domesticus
Length: 520  
Fragment?: false
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Protein
A2AUP3
Organism: Mus musculus/domesticus
Length: 513  
Fragment?: false
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Protein
Q8BVM1
Organism: Mus musculus/domesticus
Length: 502  
Fragment?: false
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Protein
A0A087WRG0
Organism: Mus musculus/domesticus
Length: 533  
Fragment?: false
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Protein
A0A0A6YW89
Organism: Mus musculus/domesticus
Length: 327  
Fragment?: false
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Protein
C9VZF1
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: false
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Protein
Q8CDS6
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: false
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Protein
A0A087WRM7
Organism: Mus musculus/domesticus
Length: 556  
Fragment?: false
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Protein
B2Z895
Organism: Mus musculus/domesticus
Length: 366  
Fragment?: false
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Protein
A7UAK5
Organism: Mus musculus/domesticus
Length: 555  
Fragment?: false
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Protein
A2AUP5
Organism: Mus musculus/domesticus
Length: 514  
Fragment?: false
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Protein
B2Z894
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: false
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Protein
Q7TS91
Organism: Mus musculus/domesticus
Length: 526  
Fragment?: false
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Protein
A7UAK4
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
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Protein
Q6GTL7
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
B2Z893
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: false
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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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom