Version 5.4
Bos taurus Gene: NEU3
Summary
InnateDB Gene IDBG-635559.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol NEU3
Gene Name sialidase-3
Synonyms
Species Bos taurus
Ensembl Gene ENSBTAG00000025931
Encoded Proteins
IDBP-687399
sialidase-3
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 ENSG00000162139:
This gene product belongs to a family of glycohydrolytic enzymes which remove sialic acid residues from glycoproteins and glycolipids. It is localized in the plasma membrane, and its activity is specific for gangliosides. It may play a role in modulating the ganglioside content of the lipid bilayer. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 15:55029090-55043623
Strand Forward strand
Band
Transcripts
ENSBTAT00000036738 ENSBTAP00000036593
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 2 interaction(s) predicted by orthology.
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004308 exo-alpha-sialidase activity
GO:0016997 alpha-sialidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006689 ganglioside catabolic process
GO:0009313 oligosaccharide catabolic process
Cellular Component
GO:0005886 plasma membrane
Orthologs
Species
Homo sapiens
Mus musculus
Gene ID
Gene Order
ENSG00000162139
View Gene Order
ENSMUSG00000035239
View Gene Order
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_116105
Glycosphingolipid metabolism pathway
REACT_19323
Sphingolipid metabolism pathway
REACT_22258
Metabolism of lipids and lipoproteins 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_111217
Metabolism pathway
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_199008
Glycosphingolipid metabolism pathway
REACT_188937
Metabolism pathway
REACT_245163
Sphingolipid metabolism pathway
REACT_247926
Metabolism of proteins pathway
REACT_236283
Post-translational protein modification pathway
REACT_232291
Metabolism of lipids and lipoproteins pathway
REACT_237472
Asparagine N-linked glycosylation pathway
REACT_202500
Sialic acid metabolism pathway
KEGG
hsa00600
Sphingolipid metabolism pathway
hsa00511
Other glycan degradation pathway
mmu00600
Sphingolipid metabolism pathway
mmu00511
Other glycan degradation pathway
INOH
PID NCI
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene Bt.477
RefSeq NM_174122
HUGO
OMIM
CCDS
HPRD
IMGT
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