Version 5.4
Mus musculus Protein: Hibch
Summary
InnateDB Protein IDBP-153763.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Hibch
Protein Name 3-hydroxyisobutyryl-Coenzyme A hydrolase
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000045606
InnateDB Gene IDBG-153761 (Hibch)
Protein Structure
UniProt Annotation
Function Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA (By similarity). {ECO:0000250}.
Subcellular Localization Mitochondrion {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 4 experimentally validated interaction(s) in this database.
They are also associated with 4 interaction(s) predicted by orthology.
Experimentally validated
Total 4 [view]
Protein-Protein 4 [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:0003824 catalytic activity
GO:0003860 3-hydroxyisobutyryl-CoA hydrolase activity
Biological Process
GO:0006574 valine catabolic process
GO:0008152 metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:1923792
InterPro IPR001753 Crotonase superfamily
IPR029045 ClpP/crotonase-like domain
PFAM PF00378
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8QZS1
PhosphoSite PhosphoSite-Q8QZS1
TrEMBL
UniProt Splice Variant
Entrez Gene 227095
UniGene
RefSeq NP_666220
MGI ID
MGI Symbol Hibch
OMIM
CCDS CCDS14948
HPRD
IMGT
EMBL AK076038 BC026437
GenPept AAH26437 BAC36138

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