Version 5.4
Mus musculus Protein: Hagh
Summary
InnateDB Protein IDBP-622940.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Hagh
Protein Name hydroxyacyl glutathione hydrolase
Synonyms BC019817; Glo-2; Glo2; Rsp29;
Species Mus musculus
Ensembl Protein ENSMUSP00000129904
InnateDB Gene IDBG-149449 (Hagh)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
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 4 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 4 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004416 hydroxyacylglutathione hydrolase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
Biological Process
GO:0006750 glutathione biosynthetic process
Cellular Component
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID MGI:95745
InterPro IPR001279 Beta-lactamase-like
IPR017782 Hydroxyacylglutathione hydrolase
PFAM PF00753
PRINTS
PIRSF PIRSF005457
SMART SM00849
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL E9Q2H8
UniProt Splice Variant
Entrez Gene 14651
UniGene Mm.43784
RefSeq
MGI ID
MGI Symbol Hagh
OMIM
CCDS
HPRD
IMGT
EMBL AC166102
GenPept

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