Version 5.4
Mus musculus Gene: Kynu
Summary
InnateDB Gene IDBG-167886.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Kynu
Gene Name kynureninase (L-kynurenine hydrolase)
Synonyms 4432411A05Rik
Species Mus musculus
Ensembl Gene ENSMUSG00000026866
Encoded Proteins
IDBP-167888
kynureninase (L-kynurenine hydrolase)
IDBP-167892
kynureninase (L-kynurenine hydrolase)
IDBP-255158
kynureninase (L-kynurenine hydrolase)
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 ENSG00000115919:
Kynureninase is a pyridoxal-5'-phosphate (pyridoxal-P) dependent enzyme that catalyzes the cleavage of L-kynurenine and L-3-hydroxykynurenine into anthranilic and 3-hydroxyanthranilic acids, respectively. Kynureninase is involved in the biosynthesis of NAD cofactors from tryptophan through the kynurenine pathway. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2010]
Kynureninase is a pyridoxal-5\'-phosphate (pyridoxal-P) dependent enzyme that catalyzes the cleavage of L-kynurenine and L-3-hydroxykynurenine into anthranilic and 3-hydroxyanthranilic acids, respectively. Kynureninase is involved in the biosynthesis of NAD cofactors from tryptophan through the kynurenine pathway. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2010]
Gene Information
Type Protein coding
Genomic Location Chromosome 2:43555329-43682715
Strand Forward strand
Band B
Transcripts
ENSMUST00000028223 ENSMUSP00000028223
ENSMUST00000050511 ENSMUSP00000061775
ENSMUST00000112826 ENSMUSP00000108445
ENSMUST00000138540
ENSMUST00000130968
ENSMUST00000148855
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
They are also associated with 14 interaction(s) predicted by orthology.
Experimentally validated
Total 1 [view]
Protein-Protein 0
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 14 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0030170 pyridoxal phosphate binding
GO:0030429 kynureninase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0006569 tryptophan catabolic process
GO:0008152 metabolic process
GO:0009435 NAD biosynthetic process
GO:0019441 tryptophan catabolic process to kynurenine
GO:0019442 tryptophan catabolic process to acetyl-CoA
GO:0019805 quinolinate biosynthetic process
GO:0034341 response to interferon-gamma
GO:0034354 'de novo' NAD biosynthetic process from tryptophan
GO:0034516 response to vitamin B6
GO:0043420 anthranilate metabolic process
GO:0097053 L-kynurenine catabolic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
Orthologs
Species
Homo sapiens
Bos taurus
Gene ID
Gene Order
ENSG00000115919
View Gene Order
ENSBTAG00000032277
Not yet available
Pathways
NETPATH
REACTOME
REACT_188937
Metabolism pathway
REACT_232845
Metabolism of amino acids and derivatives pathway
REACT_240936
Tryptophan catabolism pathway
KEGG
mmu00380
Tryptophan metabolism pathway
INOH
PID NCI
Pathway Predictions based on Human Orthology Data
NETPATH
REACTOME
REACT_916
Tryptophan catabolism pathway
REACT_13
Metabolism of amino acids and derivatives pathway
REACT_111217
Metabolism pathway
KEGG
hsa00380
Tryptophan metabolism pathway
INOH
INOH website
Tryptophan degradation pathway
PID NCI
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene Mm.105278
RefSeq NM_001289593 NM_001289594 NM_027552 XM_006498325
OMIM
CCDS CCDS16018
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