Version 5.4
Homo sapiens Protein: ST6GALNAC3
Summary
InnateDB Protein IDBP-99790.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ST6GALNAC3
Protein Name ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000329214
InnateDB Gene IDBG-99788 (ST6GALNAC3)
Protein Structure
UniProt Annotation
Function Involved in the biosynthesis of ganglioside GD1A from GM1B. Transfers CMP-NeuAc with an alpha-2,6-linkage to GalNAc residue on NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc of glycoproteins and glycolipids. ST6GalNAcIII prefers glycolipids to glycoproteins (By similarity). {ECO:0000250}.
Subcellular Localization Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Disease Associations
Tissue Specificity
Comments
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:0008373 sialyltransferase activity
Biological Process
GO:0006486 protein glycosylation
GO:0006677 glycosylceramide metabolic process
GO:0006687 glycosphingolipid metabolic process
GO:0009100 glycoprotein metabolic process
GO:0097503 sialylation
Cellular Component
GO:0000139 Golgi membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID
InterPro IPR001675 Glycosyl transferase, family 29
PFAM PF00777
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8NDV1
PhosphoSite PhosphoSite-Q8NDV1
TrEMBL
UniProt Splice Variant
Entrez Gene 256435
UniGene Hs.738623
RefSeq NP_694541
HUGO HGNC:19343
OMIM 610133
CCDS CCDS672
HPRD 15341
IMGT
EMBL AJ507291 AK091215 AY358540 BC059363 CH471059
GenPept AAH59363 AAQ88904 BAC03611 CAD45371 EAX06388

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