Version 5.4
Mus musculus Protein: Gmpr2
Summary
InnateDB Protein IDBP-165203.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Gmpr2
Protein Name guanosine monophosphate reductase 2
Synonyms 1810008P16Rik; 5730544D12Rik; AA959850;
Species Mus musculus
Ensembl Protein ENSMUSP00000002397
InnateDB Gene IDBG-165201 (Gmpr2)
Protein Structure
UniProt Annotation
Function Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides (By similarity). {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003824 catalytic activity
GO:0003920 GMP reductase activity
GO:0046872 metal ion binding
Biological Process
GO:0006144 purine nucleobase metabolic process
GO:0009117 nucleotide metabolic process
GO:0030224 monocyte differentiation
GO:0046037 GMP metabolic process
GO:0046038 GMP catabolic process
GO:0055114 oxidation-reduction process
Cellular Component
GO:0005575 cellular_component
GO:1902560 GMP reductase complex
Protein Structure and Domains
PDB ID MGI:1917903
InterPro IPR001093 IMP dehydrogenase/GMP reductase
IPR005993 Guanosine monophosphate reductase 1
PFAM PF00478
PRINTS
PIRSF PIRSF000235
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q99L27
PhosphoSite PhosphoSite-Q99L27
TrEMBL
UniProt Splice Variant
Entrez Gene 105446
UniGene Mm.390685
RefSeq NP_818773
MGI ID
MGI Symbol Gmpr2
OMIM
CCDS CCDS27124
HPRD
IMGT
EMBL AK031004 AK075772 BC003886 BC024109 CH466535
GenPept AAH03886 AAH24109 BAC27211 BAC35946 EDL36258

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca