Version 5.4
Bos taurus Gene: ST6GALNAC5
Summary
InnateDB Gene IDBG-637733.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ST6GALNAC5
Gene Name alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5
Synonyms
Species Bos taurus
Ensembl Gene ENSBTAG00000007309
Encoded Proteins
IDBP-689759
ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5
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 ENSG00000117069:
ST6GALNAC5 belongs to a family of sialyltransferases that modify proteins and ceramides on the cell surface to alter cell-cell or cell-extracellular matrix interactions (Tsuchida et al., 2003 [PubMed 12668675]).[supplied by OMIM, Mar 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 3:67863093-68073051
Strand Reverse strand
Band
Transcripts
ENSBTAT00000009616 ENSBTAP00000009616
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0001665 alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity
GO:0008373 sialyltransferase activity
GO:0016740 transferase activity
GO:0016757 transferase activity, transferring glycosyl groups
Biological Process
GO:0006486 protein glycosylation
GO:0006688 glycosphingolipid biosynthetic process
GO:0009312 oligosaccharide biosynthetic process
GO:0097503 sialylation
Cellular Component
GO:0005794 Golgi apparatus
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0030173 integral component of Golgi membrane
Orthologs
Species
Homo sapiens
Mus musculus
Gene ID
Gene Order
ENSG00000117069
View Gene Order
ENSMUSG00000039037
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_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_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
hsa00604
Glycosphingolipid biosynthesis pathway
mmu00604
Glycosphingolipid biosynthesis pathway
INOH
PID NCI
Cross-References
SwissProt
TrEMBL F1MXN8
UniProt Splice Variant
Entrez Gene 540995
UniGene Bt.106383 Bt.109102 Bt.58716
RefSeq NM_001192804
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL DAAA02008260 DAAA02008261
GenPept
RNA Seq Atlas 540995

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