Version 5.4
Mus musculus Gene: Abhd5
Summary
InnateDB Gene IDBG-205933.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Abhd5
Gene Name abhydrolase domain containing 5
Synonyms 1300003D03Rik; 2010002J10Rik; CDS; CGI-58; IECN5; NCIE2
Species Mus musculus
Ensembl Gene ENSMUSG00000032540
Encoded Proteins
IDBP-742640
IDBP-257993
abhydrolase domain containing 5
IDBP-539908
abhydrolase domain containing 5
IDBP-536285
abhydrolase domain containing 5
IDBP-741721
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This gene does not have any Entrez summary - the following is the summary from its human ortholog ENSG00000011198:
The protein encoded by this gene belongs to a large family of proteins defined by an alpha/beta hydrolase fold, and contains three sequence motifs that correspond to a catalytic triad found in the esterase/lipase/thioesterase subfamily. It differs from other members of this subfamily in that its putative catalytic triad contains an asparagine instead of the serine residue. Mutations in this gene have been associated with Chanarin-Dorfman syndrome, a triglyceride storage disease with impaired long-chain fatty acid oxidation. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 9:122351608-122381524
Strand Forward strand
Band F4
Transcripts
ENSMUST00000035128 ENSMUSP00000135538
ENSMUST00000111497 ENSMUSP00000107123
ENSMUST00000156520 ENSMUSP00000122274
ENSMUST00000154161 ENSMUSP00000122939
ENSMUST00000176005
ENSMUST00000175973 ENSMUSP00000135807
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 7 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 7 [view]
Protein-Protein 7 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0016787 hydrolase activity
GO:0042171 lysophosphatidic acid acyltransferase activity
Biological Process
GO:0006508 proteolysis
GO:0006629 lipid metabolic process
GO:0006631 fatty acid metabolic process
GO:0006654 phosphatidic acid biosynthetic process
GO:0010891 negative regulation of sequestering of triglyceride
GO:0010898 positive regulation of triglyceride catabolic process
GO:0030154 cell differentiation
GO:0051006 positive regulation of lipoprotein lipase activity
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005811 lipid particle
GO:0005829 cytosol
GO:0043231 intracellular membrane-bounded organelle
Orthologs
Species
Homo sapiens
Bos taurus
Gene ID
Gene Order
ENSG00000011198
View Gene Order
ENSBTAG00000008416
Not yet available
Pathways
NETPATH
REACTOME
REACT_245618
Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis pathway
REACT_188937
Metabolism pathway
REACT_232291
Metabolism of lipids and lipoproteins pathway
REACT_238381
Lipid digestion, mobilization, and transport pathway
KEGG
INOH
PID NCI
Pathway Predictions based on Human Orthology Data
NETPATH
REACTOME
REACT_494
Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis pathway
REACT_22258
Metabolism of lipids and lipoproteins pathway
REACT_111217
Metabolism pathway
REACT_602
Lipid digestion, mobilization, and transport pathway
KEGG
INOH
PID NCI
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene Mm.280254
RefSeq NM_026179 XM_006512243 XM_006512244 XM_006512245
OMIM
CCDS CCDS23646
HPRD
IMGT
MGI ID
MGI Symbol
EMBL
GenPept
RNA Seq Atlas

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