Version 5.4
Mus musculus Gene: Galnt3
Summary
InnateDB Gene IDBG-174988.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Galnt3
Gene Name UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3
Synonyms
Species Mus musculus
Ensembl Gene ENSMUSG00000026994
Encoded Proteins
IDBP-174990
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3
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 ENSG00000115339:
This gene encodes UDP-GalNAc transferase 3, a member of the GalNAc-transferases family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. Individual GalNAc-transferases have distinct activities and initiation of O-glycosylation is regulated by a repertoire of GalNAc-transferases. The protein encoded by this gene is highly homologous to other family members, however the enzymes have different substrate specificities. [provided by RefSeq, Jul 2008]
This gene encodes UDP-GalNAc transferase 3, a member of the GalNAc-transferases family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. Individual GalNAc-transferases have distinct activities and initiation of O-glycosylation is regulated by a repertoire of GalNAc-transferases. The protein encoded by this gene is highly homologous to other family members, however the enzymes have different substrate specificities. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 2:66082766-66124994
Strand Reverse strand
Band C1.3
Transcripts
ENSMUST00000028378 ENSMUSP00000028378
ENSMUST00000155453
ENSMUST00000150793
ENSMUST00000153563
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:0004653 polypeptide N-acetylgalactosaminyltransferase activity
GO:0005509 calcium ion binding
GO:0030145 manganese ion binding
Biological Process
GO:0018242 protein O-linked glycosylation via serine
GO:0018243 protein O-linked glycosylation via threonine
Cellular Component
GO:0005634 nucleus
GO:0005794 Golgi apparatus
GO:0016021 integral component of membrane
GO:0032580 Golgi cisterna membrane
GO:0048471 perinuclear region of cytoplasm
Orthologs
Species
Homo sapiens
Bos taurus
Gene ID
Gene Order
ENSG00000115339
View Gene Order
ENSBTAG00000013957
Not yet available
Pathways
NETPATH
REACTOME
REACT_198517
O-linked glycosylation of mucins pathway
REACT_247926
Metabolism of proteins pathway
REACT_236283
Post-translational protein modification pathway
REACT_204003
O-linked glycosylation pathway
KEGG
mmu00512
Mucin type O-Glycan biosynthesis pathway
INOH
PID NCI
Pathway Predictions based on Human Orthology Data
NETPATH
REACTOME
REACT_115606
O-linked glycosylation of mucins pathway
REACT_22161
Post-translational protein modification pathway
REACT_200727
O-linked glycosylation pathway
REACT_17015
Metabolism of proteins pathway
KEGG
hsa00512
Mucin type O-Glycan biosynthesis pathway
INOH
PID NCI
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene Mm.439760
RefSeq NM_015736
OMIM
CCDS CCDS16075
HPRD
IMGT
MGI ID
MGI Symbol
EMBL
GenPept
RNA Seq Atlas

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