Version 5.4
Mus musculus Protein: Galnt14
Summary
InnateDB Protein IDBP-255680.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Galnt14
Protein Name UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 14
Synonyms 0610033M06Rik;
Species Mus musculus
Ensembl Protein ENSMUSP00000108210
InnateDB Gene IDBG-197416 (Galnt14)
Protein Structure
UniProt Annotation
Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney (By similarity). {ECO:0000250}.
Subcellular Localization Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
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.
They are also associated with 1 interaction(s) predicted by orthology.
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0004653 polypeptide N-acetylgalactosaminyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006486 protein glycosylation
GO:0008150 biological_process
Cellular Component
GO:0000139 Golgi membrane
GO:0005575 cellular_component
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1918935
InterPro IPR001173 Glycosyltransferase 2-like
IPR029044 Nucleotide-diphospho-sugar transferases
PFAM PF00535
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8BVG5
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 71685
UniGene Mm.271953
RefSeq XP_006525002
MGI ID
MGI Symbol Galnt14
OMIM
CCDS
HPRD
IMGT
EMBL AB175681 AK002747 AK078292
GenPept BAB22325 BAC37208 BAD52069

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