Version 5.4
Homo sapiens Protein: PRPS2
Summary
InnateDB Protein IDBP-44131.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PRPS2
Protein Name phosphoribosyl pyrophosphate synthetase 2
Synonyms PRSII;
Species Homo sapiens
Ensembl Protein ENSP00000370043
InnateDB Gene IDBG-44129 (PRPS2)
Protein Structure
UniProt Annotation
Function Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 15 experimentally validated interaction(s) in this database.
Experimentally validated
Total 15 [view]
Protein-Protein 12 [view]
Protein-DNA 2 [view]
Protein-RNA 1 [view]
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0000287 magnesium ion binding
GO:0004749 ribose phosphate diphosphokinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0006015 5-phosphoribose 1-diphosphate biosynthetic process
GO:0006139 nucleobase-containing compound metabolic process
GO:0009116 nucleoside metabolic process
GO:0009165 nucleotide biosynthetic process
GO:0016310 phosphorylation
Cellular Component
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR000836 Phosphoribosyltransferase domain
IPR005946 Ribose-phosphate diphosphokinase
IPR029057 Phosphoribosyltransferase-like
PFAM PF00156
PF14572
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P11908
PhosphoSite PhosphoSite-P11908
TrEMBL
UniProt Splice Variant
Entrez Gene 5634
UniGene Hs.672215
RefSeq NP_002756
HUGO HGNC:9465
OMIM 311860
CCDS CCDS14150
HPRD 02414
IMGT
EMBL BC030019 BC040483 BC110875 BC119662 BC119663 D28134 Y00971
GenPept AAH30019 AAH40483 AAI10876 AAI19663 AAI19664 BAA05676 CAA68785

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