Version 5.4
Mus musculus Protein: Ppapdc1b
Summary
InnateDB Protein IDBP-144075.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ppapdc1b
Protein Name phosphatidic acid phosphatase type 2 domain containing 1B
Synonyms 1810019D05Rik; 2310022A04Rik; AW045471; Ppapdc1;
Species Mus musculus
Ensembl Protein ENSMUSP00000067035
InnateDB Gene IDBG-144071 (Ppapdc1b)
Protein Structure
UniProt Annotation
Function Displays magnesium-independent phosphatidate phosphatase activity in vitro. Catalyzes the conversion of phosphatidic acid to diacylglycerol (By similarity). {ECO:0000250}.
Subcellular Localization Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
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:0003824 catalytic activity
GO:0008195 phosphatidate phosphatase activity
Biological Process
GO:0046839 phospholipid dephosphorylation
Cellular Component
GO:0005575 cellular_component
GO:0016020 membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1919160
InterPro IPR000326 Phosphatidic acid phosphatase type 2/haloperoxidase
PFAM PF01569
PRINTS
PIRSF
SMART SM00014
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3UMZ3
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 71910
UniGene Mm.385055
RefSeq NP_082276
MGI ID
MGI Symbol Ppapdc1b
OMIM
CCDS CCDS40306
HPRD
IMGT
EMBL AK144593 BC099489
GenPept AAH99489 BAE25955

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