Version 5.4
Homo sapiens Gene: ST8SIA2
Summary
InnateDB Gene IDBG-30945.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ST8SIA2
Gene Name ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2
Synonyms HsT19690; SIAT8B; ST8SIA-II; STX
Species Homo sapiens
Ensembl Gene ENSG00000140557
Encoded Proteins
IDBP-30947
ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2
IDBP-600072
ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2
IDBP-601799
ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary The protein encoded by this gene is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. The encoded protein may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 15:92393828-92468728
Strand Forward strand
Band q26.1
Transcripts
ENST00000268164 ENSP00000268164
ENST00000539113 ENSP00000437382
ENST00000555434 ENSP00000450851
ENST00000556382
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
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
GO:0033691 sialic acid binding
Biological Process
GO:0001574 ganglioside biosynthetic process
GO:0005975 carbohydrate metabolic process
GO:0006464 cellular protein modification process
GO:0006486 protein glycosylation
GO:0006491 N-glycan processing
GO:0007399 nervous system development
GO:0007411 axon guidance
GO:0009311 oligosaccharide metabolic process
GO:0018279 protein N-linked glycosylation via asparagine
GO:0043687 post-translational protein modification
GO:0044267 cellular protein metabolic process
GO:0097503 sialylation
Cellular Component
GO:0000139 Golgi membrane
GO:0005769 early endosome
GO:0030173 integral component of Golgi membrane
GO:0055037 recycling endosome
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000025789
View Gene Order
ENSBTAG00000017896
Not yet available
Pathways
NETPATH
REACTOME
REACT_25085
N-Glycan antennae elongation pathway
REACT_25046
Transport to the Golgi and subsequent modification pathway
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_18312
NCAM1 interactions pathway
REACT_18334
NCAM signaling for neurite out-growth pathway
REACT_111045
Developmental Biology pathway
REACT_22161
Post-translational protein modification pathway
REACT_25208
N-glycan antennae elongation in the medial/trans-Golgi pathway
REACT_22387
Synthesis of substrates in N-glycan biosythesis pathway
REACT_18266
Axon guidance pathway
REACT_200874
Sialic acid metabolism pathway
REACT_17015
Metabolism of proteins pathway
KEGG
INOH
PID NCI
Cross-References
SwissProt
TrEMBL C6G488
UniProt Splice Variant
Entrez Gene 8128
UniGene Hs.302341
RefSeq NM_006011
HUGO HGNC:10870
OMIM 602546
CCDS CCDS10372
HPRD 03969
IMGT
EMBL AC090985 AC116162 FJ515842
GenPept ACS13735
RNA Seq Atlas 8128

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