Version 5.4
Homo sapiens Protein: LYPLAL1
Summary
InnateDB Protein IDBP-106717.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol LYPLAL1
Protein Name lysophospholipase-like 1
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000355895
InnateDB Gene IDBG-106715 (LYPLAL1)
Protein Structure
UniProt Annotation
Function Has depalmitoylating activity toward KCNMA1. Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site. {ECO:0000269PubMed:22052940, ECO:0000269PubMed:22399288}.
Subcellular Localization Isoform 1: Cytoplasm, cytosol {ECO:0000269PubMed:22399288}.Isoform 2: Cytoplasm, cytosol {ECO:0000269PubMed:22399288}.
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.
Experimentally validated
Total 2 [view]
Protein-Protein 2 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0004622 lysophospholipase activity
GO:0016787 hydrolase activity
Biological Process
GO:0002084 protein depalmitoylation
GO:0008150 biological_process
GO:0042997 negative regulation of Golgi to plasma membrane protein transport
Cellular Component
GO:0005829 cytosol
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR000801 Putative esterase
IPR002925 Dienelactone hydrolase
IPR003140 Phospholipase/carboxylesterase/thioesterase
IPR029058 Alpha/Beta hydrolase fold
PFAM PF00756
PF01738
PF02230
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q5VWZ2
PhosphoSite PhosphoSite-Q5VWZ2
TrEMBL
UniProt Splice Variant
Entrez Gene 127018
UniGene Hs.694562
RefSeq NP_620149
HUGO HGNC:20440
OMIM
CCDS CCDS1522
HPRD 14335
IMGT
EMBL AK291542 AL360093 AY341430 BC016711
GenPept AAH16711 AAQ17077 BAF84231 CAH70459 CAH70460

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