Version 5.4
Bos taurus Protein: PNP
Summary
InnateDB Protein IDBP-698819.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PNP
Protein Name Purine nucleoside phosphorylase
Synonyms NP;
Species Bos taurus
Ensembl Protein ENSBTAP00000016346
InnateDB Gene IDBG-646049 (PNP)
Protein Structure
UniProt Annotation
Function The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. {ECO:0000269PubMed:7607309}.
Subcellular Localization Cytoplasm, cytoskeleton {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0016740 transferase activity
GO:0016757 transferase activity, transferring glycosyl groups
GO:0016763 transferase activity, transferring pentosyl groups
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0009116 nucleoside metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
Protein Structure and Domains
PDB ID
InterPro IPR000845 Nucleoside phosphorylase domain
IPR011268 Purine nucleoside phosphorylase
IPR011270 Purine nucleoside phosphorylase I, inosine/guanosine-specific
PFAM PF01048
PRINTS
PIRSF PIRSF000477
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P55859
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 790312
UniGene Bt.65253
RefSeq NP_001007819
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC103291 BT021545
GenPept AAI03292 AAX46392

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