Version 5.4
Mus musculus Gene: St8sia1
Summary
InnateDB Gene IDBG-197280.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol St8sia1
Gene Name ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1
Synonyms 9330109E03Rik; GD3S; Sia-T; Siat8; Siat8a
Species Mus musculus
Ensembl Gene ENSMUSG00000030283
Encoded Proteins
IDBP-197282
ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1
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 ENSG00000111728:
Gangliosides are membrane-bound glycosphingolipids containing sialic acid. Ganglioside GD3 is known to be important for cell adhesion and growth of cultured malignant cells. The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to GM3 to produce gangliosides GD3 and GT3. The encoded protein may be found in the Golgi apparatus and is a member of glycosyltransferase family 29. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 6:142821545-142964452
Strand Reverse strand
Band G3
Transcripts
ENSMUST00000032421 ENSMUSP00000032421
ENSMUST00000147058
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 2 experimentally validated interaction(s) in this database.
Experimentally validated
Total 2 [view]
Protein-Protein 0
Protein-DNA 2 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003828 alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity
GO:0008373 sialyltransferase activity
Biological Process
GO:0006486 protein glycosylation
GO:0006665 sphingolipid metabolic process
GO:0008284 positive regulation of cell proliferation
GO:0034605 cellular response to heat
GO:0097503 sialylation
Cellular Component
GO:0030173 integral component of Golgi membrane
Orthologs
Species
Homo sapiens
Bos taurus
Gene ID
Gene Order
ENSG00000111728
View Gene Order
ENSBTAG00000000593
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
mmu00601
Glycosphingolipid biosynthesis pathway
mmu00604
Glycosphingolipid biosynthesis pathway
mmu00603
Glycosphingolipid biosynthesis 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
KEGG
hsa00604
Glycosphingolipid biosynthesis pathway
hsa00601
Glycosphingolipid biosynthesis pathway
hsa00603
Glycosphingolipid biosynthesis pathway
INOH
PID NCI
Cross-References
SwissProt Q64687
TrEMBL Q3V3B1 Q9EPK0
UniProt Splice Variant
Entrez Gene 20449
UniGene Mm.260838 Mm.445650 Mm.454279
RefSeq NM_011374 XM_006506928 XM_006506929 XM_006506930
OMIM
CCDS CCDS20689
HPRD
IMGT
MGI ID MGI:106011
MGI Symbol St8sia1
EMBL AJ401102 AK042207 BC024821 CH466572 X84235
GenPept AAH24821 BAE20627 CAA59014 CAC20706 EDL10653
RNA Seq Atlas 20449

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