Version 5.4
Mus musculus Protein: Nudt19
Summary
InnateDB Protein IDBP-174500.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Nudt19
Protein Name nudix (nucleoside diphosphate linked moiety X)-type motif 19
Synonyms D7Rp2; D7Rp2-r; D7Rp2-s; D7Rp2e; RP2-r; RP2-s;
Species Mus musculus
Ensembl Protein ENSMUSP00000047778
InnateDB Gene IDBG-174498 (Nudt19)
Protein Structure
UniProt Annotation
Function Acyl-CoA diphosphatase that mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters. At low substrate concentrations medium and long-chain fatty-acyl-CoA esters are the primary substrates. {ECO:0000269PubMed:16185196}.
Subcellular Localization Peroxisome {ECO:0000269PubMed:16185196}. Mitochondrion {ECO:0000269PubMed:16185196}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 2 experimentally validated interaction(s) in this database.
They are also associated with 5 interaction(s) predicted by orthology.
Experimentally validated
Total 2 [view]
Protein-Protein 2 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 5 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005102 receptor binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0008152 metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005777 peroxisome
Protein Structure and Domains
PDB ID MGI:94203
InterPro IPR000086 NUDIX hydrolase domain
IPR015797 NUDIX hydrolase domain-like
PFAM PF00293
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P11930
PhosphoSite PhosphoSite-P11930
TrEMBL
UniProt Splice Variant
Entrez Gene 110959
UniGene Mm.480563
RefSeq NP_149071
MGI ID
MGI Symbol Nudt19
OMIM
CCDS CCDS21152
HPRD
IMGT
EMBL BC138674 BC138675 X04097
GenPept AAI38675 AAI38676 CAA27722

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