Version 5.4
Homo sapiens Protein: GMPR
Summary
InnateDB Protein IDBP-63078.4
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol GMPR
Protein Name guanosine monophosphate reductase
Synonyms GMPR1;
Species Homo sapiens
Ensembl Protein ENSP00000259727
InnateDB Gene IDBG-63076 (GMPR)
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.
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:0009409 response to cold
GO:0043101 purine-containing compound salvage
GO:0044281 small molecule metabolic process
GO:0055086 nucleobase-containing small molecule metabolic process
GO:0055114 oxidation-reduction process
Cellular Component
GO:0005829 cytosol
GO:1902560 GMP reductase complex
Protein Structure and Domains
PDB ID
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 P36959
PhosphoSite PhosphoSite-P36959
TrEMBL
UniProt Splice Variant
Entrez Gene 2766
UniGene Hs.484741
RefSeq NP_006868
HUGO HGNC:4376
OMIM 139265
CCDS CCDS4537
HPRD 00754
IMGT
EMBL AL009031 AL138883 BC008281 L35304 M24470 M27941
GenPept AAA52498 AAA52503 AAA53106 AAH08281 CAI19917 CAI21422

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