Version 5.4
Mus musculus Protein: Ppt2
Summary
InnateDB Protein IDBP-627517.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ppt2
Protein Name palmitoyl-protein thioesterase 2
Synonyms 0610007M19Rik; AA672937;
Species Mus musculus
Ensembl Protein ENSMUSP00000131243
InnateDB Gene IDBG-172422 (Ppt2)
Protein Structure
UniProt Annotation
Function Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S- thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins (By similarity). {ECO:0000250}.
Subcellular Localization Lysosome {ECO:0000269PubMed:14528005}.
Disease Associations
Tissue Specificity Expressed throughout the brain, primarily in neurons, and at lower levels in glial cells. {ECO:0000269PubMed:11717424, ECO:0000269PubMed:14528005}.
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 24 interaction(s) predicted by orthology.
Predicted by orthology
Total 24 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0008474 palmitoyl-(protein) hydrolase activity
Biological Process
GO:0006464 cellular protein modification process
GO:0008152 metabolic process
Cellular Component
GO:0005764 lysosome
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:1860075
InterPro IPR002472 Palmitoyl protein thioesterase
IPR029058 Alpha/Beta hydrolase fold
PFAM PF02089
PRINTS PR00414
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt O35448
PhosphoSite PhosphoSite-
TrEMBL G5E8W7
UniProt Splice Variant
Entrez Gene 54397
UniGene Mm.373627
RefSeq NP_062314
MGI ID
MGI Symbol Ppt2
OMIM
CCDS CCDS28652
HPRD
IMGT
EMBL AF030001 BC013462 BC052330 CT009767
GenPept AAB82011 AAH13462 AAH52330

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