Version 5.4
Mus musculus Protein: Ptplad2
Summary
InnateDB Protein IDBP-162112.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ptplad2
Protein Name protein tyrosine phosphatase-like A domain containing 2
Synonyms 4933428I03Rik; HACD4;
Species Mus musculus
Ensembl Protein ENSMUSP00000030221
InnateDB Gene IDBG-162108 (Ptplad2)
Protein Structure
UniProt Annotation
Function Responsible for the dehydration step in very long-chain fatty acid (VLCFA) synthesis. {ECO:0000250}.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0016829 lyase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0008150 biological_process
Cellular Component
GO:0005575 cellular_component
GO:0005789 endoplasmic reticulum membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1914025
InterPro IPR007482 Protein-tyrosine phosphatase-like, PTPLA
PFAM PF04387
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt A2AKM2
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 66775
UniGene Mm.416413
RefSeq NP_080036
MGI ID
MGI Symbol Ptplad2
OMIM
CCDS CCDS18317
HPRD
IMGT
EMBL AK016968 AK017257 AK039344 AK039602 AK048282 AK050927 AL772316 BC020155
GenPept AAH20155 BAB30529 BAB30656 BAC30324 BAC30396 BAC33294 BAC34463 CAM17296 CAM17297

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