Version 5.4
Mus musculus Gene: Npl
Summary
InnateDB Gene IDBG-199157.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Npl
Gene Name N-acetylneuraminate pyruvate lyase
Synonyms 0610033B02Rik
Species Mus musculus
Ensembl Gene ENSMUSG00000042684
Encoded Proteins
IDBP-199159
N-acetylneuraminate pyruvate lyase
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 ENSG00000135838:
This gene encodes a member of the N-acetylneuraminate lyase sub-family of (beta/alpha)(8)-barrel enzymes. N-acetylneuraminate lyases regulate cellular concentrations of N-acetyl-neuraminic acid (sialic acid) by mediating the reversible conversion of sialic acid into N-acetylmannosamine and pyruvate. A pseudogene of this gene is located on the short arm of chromosome 2. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jan 2011]
Gene Information
Type Protein coding
Genomic Location Chromosome 1:153503015-153550045
Strand Reverse strand
Band G3
Transcripts
ENSMUST00000041874 ENSMUSP00000037454
ENSMUST00000187747
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0008747 N-acetylneuraminate lyase activity
GO:0016829 lyase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0008152 metabolic process
GO:0019262 N-acetylneuraminate catabolic process
Cellular Component
GO:0005575 cellular_component
GO:0005737 cytoplasm
Orthologs
Species
Homo sapiens
Bos taurus
Gene ID
Gene Order
ENSG00000135838
View Gene Order
ENSBTAG00000002266
Not yet available
Pathways
NETPATH
REACTOME
REACT_248642
Synthesis of substrates in N-glycan biosythesis pathway
REACT_262413
Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein pathway
REACT_247926
Metabolism of proteins pathway
REACT_236283
Post-translational protein modification pathway
REACT_237472
Asparagine N-linked glycosylation pathway
REACT_202500
Sialic acid metabolism pathway
KEGG
mmu00520
Amino sugar and nucleotide sugar metabolism pathway
INOH
PID NCI
Pathway Predictions based on Human Orthology Data
NETPATH
REACTOME
REACT_22433
Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein pathway
REACT_22426
Asparagine N-linked glycosylation pathway
REACT_22161
Post-translational protein modification pathway
REACT_22387
Synthesis of substrates in N-glycan biosythesis pathway
REACT_200874
Sialic acid metabolism pathway
REACT_17015
Metabolism of proteins pathway
REACT_223866
Asparagine N-linked glycosylation pathway
REACT_213782
Metabolism of proteins pathway
REACT_214405
Post-translational protein modification pathway
REACT_213420
Sialic acid metabolism pathway
REACT_220681
Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein pathway
REACT_226954
Synthesis of substrates in N-glycan biosythesis pathway
KEGG
hsa00520
Amino sugar and nucleotide sugar metabolism pathway
INOH
PID NCI
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene
RefSeq NM_028749
OMIM
CCDS CCDS15374
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