Version 5.4
Mus musculus Protein: Xpnpep3
Summary
InnateDB Protein IDBP-164721.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Xpnpep3
Protein Name X-prolyl aminopeptidase (aminopeptidase P) 3, putative
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000038331
InnateDB Gene IDBG-164719 (Xpnpep3)
Protein Structure
UniProt Annotation
Function
Subcellular Localization Mitochondrion {ECO:0000269PubMed:20179356}.
Disease Associations
Tissue Specificity Expressed in brain, kidney, heart, liver, skeletal muscle and testis. {ECO:0000269PubMed:20179356}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 5 experimentally validated interaction(s) in this database.
They are also associated with 6 interaction(s) predicted by orthology.
Experimentally validated
Total 5 [view]
Protein-Protein 5 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 6 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004177 aminopeptidase activity
GO:0030145 manganese ion binding
Biological Process
GO:0003094 glomerular filtration
GO:0006508 proteolysis
GO:0016485 protein processing
Cellular Component
GO:0005739 mitochondrion
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:2445217
InterPro IPR000994 Peptidase M24, structural domain
IPR007865 Aminopeptidase P, N-terminal
IPR028980 Creatinase/Aminopeptidase P, N-terminal
PFAM PF00557
PF05195
PRINTS
PIRSF
SMART SM01011
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt B7ZMP1
PhosphoSite PhosphoSite-B7ZMP1
TrEMBL
UniProt Splice Variant
Entrez Gene 321003
UniGene Mm.410525
RefSeq NP_796284
MGI ID
MGI Symbol Xpnpep3
OMIM
CCDS CCDS27668
HPRD
IMGT
EMBL AK088324 BC137569 BC144717 CH466550
GenPept AAI37570 AAI44718 BAC40282 EDL04573 EDL04574

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