Version 5.4
Mus musculus Protein: Upp2
Summary
InnateDB Protein IDBP-172226.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Upp2
Protein Name uridine phosphorylase 2
Synonyms 1700124F02Rik; AI266885; UDRPASE2; UP2; UPASE2;
Species Mus musculus
Ensembl Protein ENSMUSP00000099816
InnateDB Gene IDBG-172222 (Upp2)
Protein Structure
UniProt Annotation
Function Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1- phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (By similarity). {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity Liver specific.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003824 catalytic activity
GO:0004850 uridine phosphorylase activity
Biological Process
GO:0009116 nucleoside metabolic process
GO:0009166 nucleotide catabolic process
GO:0044206 UMP salvage
Cellular Component
GO:0005737 cytoplasm
GO:0045098 type III intermediate filament
Protein Structure and Domains
PDB ID MGI:1923904
InterPro IPR000845 Nucleoside phosphorylase domain
IPR010059 Uridine phosphorylase, eukaryotic
PFAM PF01048
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8CGR7
PhosphoSite PhosphoSite-Q8CGR7
TrEMBL Q3UEN1
UniProt Splice Variant
Entrez Gene 76654
UniGene Mm.378432
RefSeq NP_083968
MGI ID
MGI Symbol Upp2
OMIM
CCDS CCDS16051
HPRD
IMGT
EMBL AK149444 AY152393 CH466519
GenPept AAO05705 BAE28880 EDL26945

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